spacer
spacer

PDBsum entry 2jqv

Go to PDB code: 
protein links
Structural genomics PDB id
2jqv
Jmol
Contents
Protein chain
165 a.a. *
* Residue conservation analysis
PDB id:
2jqv
Name: Structural genomics
Title: Solution structure at3g28950.1 from arabidopsis thaliana
Structure: Aig2 protein-like. Chain: a. Synonym: at3g28950. Engineered: yes
Source: Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Gene: at3g28950.1. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: B.F.Volkman,N.B.De La Cruz,F.C.Peterson,Center For Eukaryotic Structural Genomics (Cesg)
Key ref:
N.B.de la Cruz et al. (2008). Solution structure of At3g28950 from Arabidopsis thaliana. Proteins, 71, 546-551. PubMed id: 18214976 DOI: 10.1002/prot.21936
Date:
07-Jun-07     Release date:   14-Aug-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9MBH1  (Q9MBH1_ARATH) -  AIG2 protein-like
Seq:
Struc:
165 a.a.
165 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cellular_component   1 term 
  Biological process     biological_process   1 term 

 

 
DOI no: 10.1002/prot.21936 Proteins 71:546-551 (2008)
PubMed id: 18214976  
 
 
Solution structure of At3g28950 from Arabidopsis thaliana.
N.B.de la Cruz, F.C.Peterson, B.F.Volkman.
 
  ABSTRACT  
 
We determined the solution structure of At3g28950 from A. thaliana, a homolog of At5g39720, whose structure we solved earlier. The secondary structure of the 165-aa protein consists of a 5-strand antiparallel beta-barrel domain flanked by two alpha-helices and a 2-strand beta-sheet; an additional free C-terminal alpha-helix extends into solution. Bioinformatic searches and analyses suggest that members of this growing set of structurally related proteins have been recruited to serve a wide variety of functions ranging from gamma-glutamyl cyclotransferase activity to participation in plant responses to chemical and biotic stimuli. Expression of a human homolog is elevated in bladder cancer tissues. Expression patterns for At3g28950 and its Arabidopsis paralogs suggest that each one evolved a different physiological role. The At3g28950 structure was solved as part of a structural genomics effort, and the results demonstrate how such a project can further understanding of genome evolution in addition to sequence-structure and structure-function relationships. Proteins 2008. (c) 2008 Wiley-Liss, Inc.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. (A) ^15N-^1H HSQC spectrum of At3g28950. Representative resonance assignments are indicated by residue number and one-letter amino acid code. (B) Stereoview of the ensemble of 20 At3g28950 conformers. Secondary structure elements are colored cyan (helix) or magenta ( -sheet). (C) Ribbon diagram of At3g38950 with -helices and -strands shown in cyan and magenta, respectively. A portion of the flexible C-terminal helix (white) is omitted for clarity. Residue ranges for secondary structure elements include: 1(19-27), 2(71-81), 3(122-147), 4(152-157), 1(9-13), 2(32-39), 3(42-43), 4(54-55), 5(61-70), 6(86-95), and 7(101-109). (D) Backbone RMSD values for At3g28950 ensemble and (E) ^15N-^1H heteronuclear NOE values are plotted as a function of amino acid sequence.
Figure 2.
Figure 2. (A) At3g28950 (red) and structural homologs At5g39720 (blue) and C7orf24 from Homo sapiens (PDB code 2I5T). (B) ClustalW[18] alignment of sequences for At3g28950, At5g39720, and human C7orf24.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2008, 71, 546-551) copyright 2008.